Cathepsin C - Revision history

Wu3857: /* Protein Function */

2019-08-20T04:30:32Z

‎Protein Function

Wu3857: /* Cys Function & Property */

2019-08-20T04:30:16Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|Dipeptidyl peptidase 1, CTSC, DPP-I|[https://www.uniprot.org/uniprot/P53634 P53634]|Homo sapiens|Cys258|[http:/..."

2019-08-20T04:29:36Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Dipeptidyl peptidase 1, CTSC, DPP-I|[https://www.uniprot.org/uniprot/P53634 P53634]|Homo sapiens|Cys258|[http:/..."

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{{#invoke:InfoboxforTarget|run|Dipeptidyl peptidase 1, CTSC, DPP-I|[https://www.uniprot.org/uniprot/P53634 P53634]|Homo sapiens|Cys258|[http://pfam.xfam.org/family/PF00112 Peptidase C1 family]|[[:Category:Cathepsin C|Ligand list]]|Protease}}
==Summary==

===Protein Function ===
Cathepsin C (CatC or dipeptidyl peptidase I) is a lysosomal cysteine protease which could act as both an exopeptidase and endopeptidase. It is important for intracellular protein degradation and plays a key role in the activation of the proinflammatory serine proteases neutrophil elastase (NE), cathepsin G (CatG), and proteinase-3 (PR-3). CatC can also activate neuraminidase and factor XIII. In humans, CatC mutations are associated with the autosomal recessive disorders Haim−Munck syndrome and Papillon−Lefèvre syndrome, both associated with almost complete loss of the secondary enzymatic activities of all three serine proteases, NE, CatG, and PR-3, in neutrophils and granzyme B in NK cells and characterized by palmoplantar keratosis and severe childhood periodontal disease. (From Uniprot, PMID: 24592859) 

===Cys Function & Property===
Cys258 is one of the active sites of CatC. The "CGSC" motif is very conserved in peptidase family. 

* Hydrophobic property:
:[[File:578-hydro.png||600px]]
* SASA:
:Cys258: 10.925 A^2 

==Protein Sequence==

MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR 
DVNCSVMGPQ EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK 
WFAFFKYKEE GSKVTTYCNE TMTGWVHDVL GRNWACFTGK KVGTASENVY 
VNIAHLKNSQ EKYSNRLYKY DHNFVKAINA IQKSWTATTY MEYETLTLGD 
MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV HGINFVSPVR 
NQASCGS'''C'''YS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG 
GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG 
FYGGCNEALM KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF 
ELTNHAVLLV GYGTDSASGM DYWIVKNSWG TGWGENGYFR IRRGTDECAI 
ESIAVAATPI PKL 


==Structural Information==
*Known structure with covalent ligand: 
:[https://www.rcsb.org/structure/2DJF 2DJF], [https://www.rcsb.org/structure/3PDF 3PDF], [https://www.rcsb.org/structure/4CDC 4CDC], [https://www.rcsb.org/structure/4CDE 4CDE], [https://www.rcsb.org/structure/4CDF 4CDF], [https://www.rcsb.org/structure/4CDD 4CDD] 

*Protein structure:
:[[File:578.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04142 Lysosome] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis] 

==Experimental Evidence==
:Molecular Docking, Homologous Analysis of Sequence

==Reference==
# Mølgaard A, Arnau J, Lauritzen C, et al. '''The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2[J].''' Biochemical Journal, 2007, 401(3): 645-650. [https://www.ncbi.nlm.nih.gov/pubmed/?term=17020538 17020538] 
# Furber M, Tiden A K, Gardiner P, et al. '''Cathepsin C inhibitors: property optimization and identification of a clinical candidate[J].''' Journal of medicinal chemistry, 2014, 57(6): 2357-2367. [https://www.ncbi.nlm.nih.gov/pubmed/?term=24592859 24592859] 
# Méthot N, Rubin J, Guay D, et al. '''Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing[J].''' Journal of Biological Chemistry, 2007, 282(29): 20836-20846. [https://www.ncbi.nlm.nih.gov/pubmed/?term=17535802 17535802] 

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Protease]]
[[Category:Peptidase C1 family]]
[[Category:Lysosome]]
[[Category:Apoptosis]]

@@ Line 6: / Line 6: @@
 ===Protein Function ===
-Cathepsin C (CatC or dipeptidyl peptidase I) is a lysosomal cysteine protease which could act as both an exopeptidase and endopeptidase. It is important for intracellular protein degradation and plays a key role in the activation of the proinflammatory serine proteases neutrophil elastase (NE), cathepsin G (CatG), and proteinase-3 (PR-3). CatC can also activate neuraminidase and factor XIII. In humans, CatC mutations are associated with the autosomal recessive disorders Haim−Munck syndrome and Papillon−Lefèvre syndrome, both associated with almost complete loss of the secondary enzymatic activities of all three serine proteases, NE, CatG, and PR-3, in neutrophils and granzyme B in NK cells and characterized by palmoplantar keratosis and severe childhood periodontal disease. (From Uniprot, PMID: 24592859)<br/>
+Cathepsin C (CatC or dipeptidyl peptidase I) is a lysosomal cysteine protease which could act as both an exopeptidase and endopeptidase. It is important for intracellular protein degradation and plays a key role in the activation of the proinflammatory serine proteases neutrophil elastase (NE), cathepsin G (CatG), and proteinase-3 (PR-3).<br/>
 ===Cys Function & Property===

@@ Line 9: / Line 9: @@
 ===Cys Function & Property===
-Cys258 is one of the active sites of CatC. The "CGSC" motif is very conserved in peptidase family. <br/>
+Cys258 is one of the active sites of CatC.<br/>The CGSC sequecne beside Cys258 is very conserved in peptidase family. <br/>
 * Hydrophobic property:

Cathepsin C - Revision history

Wu3857: /* Protein Function */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Dipeptidyl peptidase 1, CTSC, DPP-I|[https://www.uniprot.org/uniprot/P53634 P53634]|Homo sapiens|Cys258|[http:/..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|Dipeptidyl peptidase 1, CTSC, DPP-I|[https://www.uniprot.org/uniprot/P53634 P53634]|Homo sapiens|Cys258|[http:/..."